Calcium in PDB 4los: C1S CUB2-CCP1

All present enzymatic activity of C1S CUB2-CCP1:
3.4.21.42;

The structure of C1S CUB2-CCP1, PDB code: 4los was solved by R.Wallis, U.Venkatraman Girija, P.C.E.Moody, J.E.Marshall, A.R.Gingras, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.49 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	66.480, 69.190, 76.650, 90.00, 90.00, 90.00
R / Rfree (%)	17.6 / 21.2

The binding sites of Calcium atom in the C1S CUB2-CCP1 (pdb code 4los). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the C1S CUB2-CCP1, PDB code: 4los:

Calcium binding site 1 out of 1 in the C1S CUB2-CCP1


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of C1S CUB2-CCP1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca401 b:39.4 occ:1.00 OE1 A:GLU211 2.2 39.8 1.0 O A:HOH501 2.2 37.1 1.0 OD1 A:ASP260 2.3 39.5 1.0 O A:GLY263 2.3 44.8 1.0 O A:THR262 2.4 41.4 1.0 OD2 A:ASP221 2.4 36.6 1.0 OD1 A:ASP221 2.6 35.7 1.0 CG A:ASP221 2.8 39.4 1.0 C A:GLY263 3.4 42.7 1.0 CD A:GLU211 3.4 49.0 1.0 C A:THR262 3.4 48.0 1.0 CG A:ASP260 3.5 35.8 1.0 CA A:GLY263 3.9 46.0 1.0 N A:ASP260 4.0 35.9 1.0 N A:GLY263 4.0 46.4 1.0 CB A:GLU211 4.1 41.2 1.0 OD2 A:ASP260 4.2 43.8 1.0 OE1 A:GLN264 4.2 46.8 1.0 OE2 A:GLU211 4.2 54.3 1.0 CB A:ASP221 4.3 34.1 1.0 O A:ASP260 4.3 39.2 1.0 CG A:GLU211 4.4 44.0 1.0 N A:THR262 4.4 45.9 1.0 C A:ASP260 4.4 36.8 1.0 N A:GLN264 4.5 45.2 1.0 OH A:TYR181 4.5 38.1 1.0 CA A:THR262 4.5 45.3 1.0 CA A:ASP260 4.5 37.3 1.0 CB A:ASP260 4.6 35.7 1.0 CB A:THR259 4.7 38.1 1.0 CE1 A:TYR181 4.7 40.1 1.0 CA A:GLN264 4.9 49.6 1.0 CD A:GLN264 4.9 46.3 1.0 C A:THR259 5.0 40.0 1.0 N A:ASP221 5.0 35.9 1.0

U.Venkatraman Girija, A.R.Gingras, J.E.Marshall, R.Panchal, M.A.Sheikh, P.Gal, W.J.Schwaeble, D.A.Mitchell, P.C.Moody, R.Wallis. Structural Basis of the C1Q/C1S Interaction and Its Central Role in Assembly of the C1 Complex of Complement Activation. Proc.Natl.Acad.Sci.Usa V. 110 13916 2013.
ISSN: ISSN 0027-8424
PubMed: 23922389
DOI: 10.1073/PNAS.1311113110